Species | Fusarium circinatum | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium circinatum | |||||||||||
CAZyme ID | KAF5659801.1 | |||||||||||
CAZy Family | AA5 | |||||||||||
CAZyme Description | death-associated kinase 1 | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 32892; End:41088 Strand: - |
MYSSSGRNLT SFRGETSDPT TFKPYDPETL DDARFIPNAL DFAYRAFLAD NAVTLSVPPV | 60 |
FSNAQAVDSA SFAGRGASFT VYRRRIPPQK TLTSRTNMDG LLIEIKDKRK LPEVVAYKVA | 120 |
LIEFSDKGEA TQTSRHAIDA AIMELYLSTH RPILQHPNLV DFLGLAWGAN PFNSSQKLPV | 180 |
LMVEFAEYGS LSQLQQREYL GVETRRKLCL DVCKGLHMLH SCGIAHGDIK AENALIFKDA | 240 |
EHKYRAKVSD FGYSQVINAE RDSLLLGGTR PWKAPEAKTA VKVSDAKYTD IYSLSLFIWC | 300 |
TFALGQNIFK LFVNPSKKGD EFYAEAEKLK ETRELAAQND ISTWYWKVIT ATTHGDTGQF | 360 |
LQHFKSLQQQ LEQLQQNTAQ ANRLEVGIDD IEKILCAIPP VSFQALEPLK QQLITTVRRL | 420 |
GSYDAMKRAV TIGLSNEPQQ RDLDQIMIAL GHSGSFTEDS VEPNQVLKSN LNQHFFTWRH | 480 |
WTGMDPSVQR YLTTTYIQRG EGEVKKGMIN PPEAFLLTAL YINGYGVDKN TSQAIRWLFN | 540 |
AWGVKHPLAS AYGYRIARAI GRTPDNPDSV IETLELMALR GSRTALEDLA TLSKDTYDKT | 600 |
KKTIRDVLGG TGANFFWKTE MLHGFAHNMW IRTFENIPIM LENFSQFDSI AEYTANKRGD | 660 |
RILHVAASCG QTEAIRALLN HFPSLEVNQL NDQGETPLLC ACRAGQHDTV MWLTSNGATA | 720 |
SAARNGESPL HWLISFDDEE VESVGLSLIQ AGADTNAKTT TFIAYQGSFP ASLDVDRLPE | 780 |
GYPIGWATHC SRPKIVKFLL SHTADPRMCN KSWPRARSAL ETAASQLRSE CLELMIHAIE | 840 |
YFNLEQGAEK HGGFLVTSLL QQAVYGTSLF DMILYHGPRY QQAMEYTFQC LLPRTSRVAS | 900 |
PNGYGGFNQT LLYLAVSLAR DELAEYLLKH GADVMKTGEN YDEQILQSQD VGAFKTADIN | 960 |
RACGIDLRTP LLEAVRWNRP TMVNLLLEHG AHATEASNNP FSGQASTWTA LHVLAHAGQN | 1020 |
DTRLVQPLLD HGAPLDGFPD EVGKTESPLL VAMQRDLFQL ADSFISHGAD INLTSMSSGH | 1080 |
LSFTNPTTIF GHVIASNARN SISRLRYLLG RTDCLDFIVE PTRQWTALHR AAAAHIDVEF | 1140 |
RATDATEAAE LDWTDIDWSA NREIMNELLR QFDDPEQVGS VEGSMGLTAM HLAVLAGNDG | 1200 |
AVKLLLDKGA RSDVRSADGK GPTAAEMVFG IQMERLSIIE EGARPGKEEV AALPMRLYGC | 1260 |
QSLAYTAAIS AVLGQGISPL SDAVQGFAAP AAEYRPKFRY WLPDADVDHD VLKTDIQDLQ | 1320 |
KLGAGGLEFL PFYNYGFGGV NDSKMETYAF GKPAFRDVLQ IALEATKANG LSMDVALGAS | 1380 |
QGQGVPSKPL TPGLAVQLVY GKVSVKGGEK FDGALPATDI NWNENLGYIH PQEKFGGNRL | 1440 |
IGVSAAAVAS KNASDESNIF VSLHEKSLVD LSNNVKNGKL TWTAPKDYKE YVLFAHYERY | 1500 |
TNQRSCDGVP TDVIANGSWV TDHFSAAGAK LASQFWEKNL LSTQIRQLLK DVGKHTWEDS | 1560 |
MEIQASLYWS PGFPDRFKSK RGYNVIKYLP LLFHKSTSFT AAQAPYNTTF YLDGTPDDGQ | 1620 |
SKYLQDYRLT LNDGYQEYLQ TFEEWAESLG LSHSCQVGYN IPLDILADVP IVSTPELESL | 1680 |
AFKTPDQMSQ FVSPAHLGRR NVISTEIGAV PQGAYSLTIP SLVNLFHDAF AGGVNAMMIH | 1740 |
GMTYTGEQLG SAWPGFTPFQ YIYTELWSPK QPAWKYMGDM MNYTARNQFV LQQGVAKKDL | 1800 |
AFYLYKDPFG ISDEYNGTDL RASGFTYEYL SPANFGSKVL KVTNKNLDSA GAGYRALVLD | 1860 |
QQQFITADAS QKLVELADAG LPLVVIGDLP TTAIGTKGKD VVTRNISKLK GPKYSNIVFI | 1920 |
KSVDDLLNAL DKLSVKPRVL TSSDAAKNLY TVWRSDKSSD YLFFFNKGPS ASFEVTAEVE | 1980 |
HGKVPYRIDA WTGQQMAMAS FKRPSGKISL QVSLKERQTA IVAFTSGKSK TSIVSQSKNV | 2040 |
LDASYGSDGK EGISVILGDA KEASLTLSNG QTKKIPAASS SGKKNALNID ISNWNLTLES | 2100 |
WVPGPNEAKS ASVKKVMKLG TQKTLKPWSE ISGAQNISGV GTYTATFRVA QLPSKDSIAV | 2160 |
LQFGPLLNTI RAWVNDKQLP AIDIYDAQVD VSDCLVKGSN TIRVEVASTL FNAVKARVDY | 2220 |
VKANGGGPAA PILYTSADWQ KHGLIGPVSI RSLRKISL | 2258 |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH106 | 1285 | 2250 | 3.4e-94 | 0.9927184466019418 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
407266 | Glyco_hydro_106 | 6.10e-25 | 1430 | 1994 | 321 | 865 | alpha-L-rhamnosidase. |
270622 | PKc | 1.09e-22 | 154 | 317 | 48 | 204 | Catalytic domain of Protein Kinases. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase. |
270901 | STKc_MAP3K-like | 2.80e-21 | 153 | 299 | 46 | 182 | Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway. |
214567 | S_TKc | 3.82e-18 | 154 | 294 | 54 | 182 | Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily. |
270910 | STKc_LKB1_CaMKK | 4.01e-18 | 154 | 322 | 61 | 230 | Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QKD46519.1|GH106 | 0.0 | 1255 | 2258 | 1 | 1021 |
QGI59730.1|GH106 | 0.0 | 1255 | 2257 | 1 | 1009 |
QGI90645.1|GH106 | 0.0 | 1255 | 2257 | 1 | 1009 |
QGI76932.1|GH106 | 0.0 | 1255 | 2258 | 1 | 1010 |
CCT63273.1|GH106 | 0.0 | 1255 | 2258 | 1 | 1010 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3SXR_A | 4.82e-12 | 154 | 314 | 60 | 211 | Crystal structure of BMX non-receptor tyrosine kinase complex with dasatinib [Homo sapiens],3SXR_B Crystal structure of BMX non-receptor tyrosine kinase complex with dasatinib [Homo sapiens],3SXS_A Crystal structure of BMX non-receptor tyrosine kinase complexed with PP2 [Homo sapiens] |
6I99_A | 5.55e-12 | 154 | 314 | 70 | 221 | Bone Marrow Tyrosine Kinase in Chromosome X in complex with a newly designed covalent inhibitor JS24 [Homo sapiens],6I99_B Bone Marrow Tyrosine Kinase in Chromosome X in complex with a newly designed covalent inhibitor JS24 [Homo sapiens] |
4ITH_A | 7.39e-10 | 154 | 303 | 70 | 223 | Crystal structure of RIP1 kinase in complex with necrostatin-1 analog [Homo sapiens],4ITH_B Crystal structure of RIP1 kinase in complex with necrostatin-1 analog [Homo sapiens],4ITI_A Crystal structure of RIP1 kinase in complex with necrostatin-3 analog [Homo sapiens],4ITI_B Crystal structure of RIP1 kinase in complex with necrostatin-3 analog [Homo sapiens],4ITJ_A Crystal structure of RIP1 kinase in complex with necrostatin-4 [Homo sapiens],4ITJ_B Crystal structure of RIP1 kinase in complex with necrostatin-4 [Homo sapiens] |
6NYH_A | 7.54e-10 | 154 | 303 | 72 | 225 | Structure of human RIPK1 kinase domain in complex with GNE684 [Homo sapiens],6NYH_B Structure of human RIPK1 kinase domain in complex with GNE684 [Homo sapiens] |
7FCZ_A | 7.62e-10 | 154 | 303 | 73 | 226 | Chain A, Receptor-interacting serine/threonine-protein kinase 1 [Homo sapiens],7FCZ_B Chain B, Receptor-interacting serine/threonine-protein kinase 1 [Homo sapiens],7FD0_A Chain A, Receptor-interacting serine/threonine-protein kinase 1 [Homo sapiens],7FD0_B Chain B, Receptor-interacting serine/threonine-protein kinase 1 [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
sp|Q7T6X2|YR826_MIMIV | 1.78e-11 | 154 | 299 | 839 | 978 | Putative serine/threonine-protein kinase/receptor R826 OS=Acanthamoeba polyphaga mimivirus OX=212035 GN=MIMI_R826 PE=3 SV=2 |
sp|Q2MHE4|HT1_ARATH | 2.01e-11 | 154 | 299 | 142 | 277 | Serine/threonine/tyrosine-protein kinase HT1 OS=Arabidopsis thaliana OX=3702 GN=HT1 PE=1 SV=1 |
sp|Q7T6Y2|YR831_MIMIV | 5.22e-11 | 154 | 299 | 838 | 978 | Putative serine/threonine-protein kinase/receptor R831 OS=Acanthamoeba polyphaga mimivirus OX=212035 GN=MIMI_R831 PE=3 SV=2 |
sp|P97504|BMX_MOUSE | 7.76e-11 | 154 | 314 | 443 | 594 | Cytoplasmic tyrosine-protein kinase BMX OS=Mus musculus OX=10090 GN=Bmx PE=2 SV=1 |
sp|P51813|BMX_HUMAN | 2.38e-10 | 154 | 314 | 467 | 618 | Cytoplasmic tyrosine-protein kinase BMX OS=Homo sapiens OX=9606 GN=BMX PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.999971 | 0.000076 |
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